Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3JYI

Structural and biochemical evidence that a TEM-1 {beta}-lactamase Asn170Gly active site mutant acts via substrate-assisted catalysis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0030655	biological_process	beta-lactam antibiotic catabolic process
A	0046677	biological_process	response to antibiotic
B	0005515	molecular_function	protein binding
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0030655	biological_process	beta-lactam antibiotic catabolic process
B	0046677	biological_process	response to antibiotic
C	0005515	molecular_function	protein binding
C	0008800	molecular_function	beta-lactamase activity
C	0016787	molecular_function	hydrolase activity
C	0017001	biological_process	antibiotic catabolic process
C	0030655	biological_process	beta-lactam antibiotic catabolic process
C	0046677	biological_process	response to antibiotic
D	0005515	molecular_function	protein binding
D	0008800	molecular_function	beta-lactamase activity
D	0016787	molecular_function	hydrolase activity
D	0017001	biological_process	antibiotic catabolic process
D	0030655	biological_process	beta-lactam antibiotic catabolic process
D	0046677	biological_process	response to antibiotic
E	0005515	molecular_function	protein binding
E	0008800	molecular_function	beta-lactamase activity
E	0016787	molecular_function	hydrolase activity
E	0017001	biological_process	antibiotic catabolic process
E	0030655	biological_process	beta-lactam antibiotic catabolic process
E	0046677	biological_process	response to antibiotic
F	0005515	molecular_function	protein binding
F	0008800	molecular_function	beta-lactamase activity
F	0016787	molecular_function	hydrolase activity
F	0017001	biological_process	antibiotic catabolic process
F	0030655	biological_process	beta-lactam antibiotic catabolic process
F	0046677	biological_process	response to antibiotic

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE A 3380

Chain	Residue
A	SER70
A	HOH313
A	TYR105
A	SER130
A	VAL216
A	LYS234
A	SER235
A	GLY236
A	ALA237
A	ARG243

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 1

Chain	Residue
A	GLU212
A	PHE230
A	ILE231

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE B 3380

Chain	Residue
B	SER70
B	SER130
B	LYS234
B	SER235
B	GLY236
B	ALA237
B	ARG243
B	HOH318

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 2

Chain	Residue
B	GLU212
B	ARG222
B	TRP229
B	ILE231

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EPE C 3380

Chain	Residue
C	SER70
C	SER130
C	LYS234
C	SER235
C	ARG243

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PO4 C 4

Chain	Residue
C	TRP165

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE D 3380

Chain	Residue
D	SER70
D	SER130
D	LYS234
D	SER235
D	GLY236
D	ALA237
D	ARG243
D	HOH303

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EPE E 3380

Chain	Residue
E	SER130
E	SER235
E	GLY236
E	HOH299

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 3

Chain	Residue
E	GLU212
E	ARG222
E	PHE230
E	ILE231

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EPE F 3380

Chain	Residue
F	SER70
F	SER130
F	LYS234
F	SER235
F	GLY236
F	ALA237
F	ARG243

Functional Information from PROSITE/UniProt

site_id	PS00146
Number of Residues	16
Details	BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL

Chain	Residue	Details
A	PHE66-LEU81

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Acyl-ester intermediate"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
A	GLU166
A	LYS73
A	SER130
A	SER70

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
B	GLU166
B	LYS73
B	SER130
B	SER70

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
C	GLU166
C	LYS73
C	SER130
C	SER70

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
D	GLU166
D	LYS73
D	SER130
D	SER70

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
E	GLU166
E	LYS73
E	SER130
E	SER70

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
F	GLU166
F	LYS73
F	SER130
F	SER70

site_id	MCSA1
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
A	SER70	electrostatic stabiliser
A	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS234	electrostatic stabiliser
A	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
B	SER70	electrostatic stabiliser
B	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLU166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LYS234	electrostatic stabiliser
B	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
C	SER70	electrostatic stabiliser
C	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLU166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	LYS234	electrostatic stabiliser
C	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
D	SER70	electrostatic stabiliser
D	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLU166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	LYS234	electrostatic stabiliser
D	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA5
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
E	SER70	electrostatic stabiliser
E	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	GLU166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	LYS234	electrostatic stabiliser
E	ALA237	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA6
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
F	SER70	electrostatic stabiliser
F	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	GLU166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	LYS234	electrostatic stabiliser
F	ALA237	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)